Related Experiment Video
Updated: May 6, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Stability and conformational change of methoxypolyethylene glycol modification for native and unfolded trypsin
Wei Liu1, Jun-Ping Liu, Li-Qiang Zou
1State Key Laboratory of Food Science and Technology, Nanchang University, No. 235, Nanjing East Road, Nanchang, Jiangxi 330047, China.
Abstract:
The effect of succinimidyl carbonates activated methoxypolyethylene glycol (mPEG-SC) on the catalytic properties and conformation of native trypsin and dynamic high-pressure microfluidisation (DHPM) induced unfolded trypsin was studied. The thermal stability of unfolded trypsin was enhanced more significantly than that of native trypsin between 45 and 70°C. The autolysis analysis indicated that modified unfolded trypsin was markedly more resistant to autolysis compared to modified native trypsin between 40 and 180min. Upon mPEG-SC conjugation, the Km value of the enzyme decreased by about 2-fold, and the catalytic efficiency (Kcat/Km) increased by about 3-4-fold. Moreover, the increased thermal stability of unfolded trypsin might be due to the lower surface hydrophobicity and the higher hydrogen bond formation after mPEG-SC modification, which was reflected in the decrease of UV absorbance, the quenching and blue shift of fluorescence spectra, as well as the increase of β-sheet content.
More Related Videos
15:33Microwave-assisted Functionalization of Polyethylene glycol and On-resin Peptides for Use in Chain Polymerizations and Hydrogel Formation
Published on: October 29, 2013
08:34OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
Published on: February 5, 2020
Related Concept Videos
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Protein Folding Quality Check in the RER
Molecular Chaperones and Protein Folding
The...
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Protein Denaturation